Akademik Veri Yönetim Sistemi
11th INTERNATIONAL CUKUROVA AGRICULTURE AND VETERINARY CONGRESS, Adana, Türkiye, 27 - 28 Aralık 2025, ss.174, (Özet Bildiri)
Within the scope of this study, the purification of polyphenol oxidase (PPO), its activity
measurements, and the synthesis processes of modified vanadium quantum dots were
investigated. PPO is an enzyme that exists in an intracellular form in banana fruit; therefore, it
was first converted into an extracellular form. Following enzyme extraction, ammonium sulfate
precipitation was applied, and the purification process was subsequently carried out using an
affinity gel with a Sepharose 4B–L-tyrosine–p-aminobenzoic acid chemical structure. The
banana fruits used in this study were imported and purchased from local markets in Kocaeli,
Türkiye. Experimental measurements were performed spectrophotometrically, and enzyme
activity was determined by evaluating the differences between absorbance values recorded at 0
and 1 minute. The inhibitory effects of modified synthesized vanadium quantum dots, coded as
DMF1–DMF9, on the PPO enzyme were investigated. Based on the experimental data,
percentage activity graphs were generated, and IC₅₀ values were calculated accordingly. In
addition, further kinetic studies were conducted using the same inhibitors to determine
inhibition types, and Ki values were calculated. According to the results obtained, the inhibitor
DMF9, with an IC₅₀ value of 1058.7 µM, exhibited the strongest inhibitory effect on the PPO
enzyme. In contrast, DMF4, which had the highest IC₅₀ value (1394.3 µM), was identified as
the weakest inhibitor. Moreover, DMF2 demonstrated the highest affinity for the enzyme,
exhibiting an uncompetitive inhibition mechanism and the lowest Ki value (553.5 µM).